ID F6SYV1_CALJA Unreviewed; 1093 AA.
AC F6SYV1;
DT 27-JUL-2011, integrated into UniProtKB/TrEMBL.
DT 25-MAY-2022, sequence version 2.
DT 27-MAR-2024, entry version 61.
DE RecName: Full=Valine--tRNA ligase, mitochondrial {ECO:0000256|ARBA:ARBA00040837};
DE EC=6.1.1.9 {ECO:0000256|ARBA:ARBA00013169};
DE AltName: Full=Valyl-tRNA synthetase {ECO:0000256|ARBA:ARBA00029936};
GN Name=VARS2 {ECO:0000313|Ensembl:ENSCJAP00000036867.3};
OS Callithrix jacchus (White-tufted-ear marmoset).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Primates; Haplorrhini; Platyrrhini; Cebidae;
OC Callitrichinae; Callithrix; Callithrix.
OX NCBI_TaxID=9483 {ECO:0000313|Ensembl:ENSCJAP00000036867.3, ECO:0000313|Proteomes:UP000008225};
RN [1] {ECO:0000313|Ensembl:ENSCJAP00000036867.3}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RA Warren W., Ye L., Minx P., Worley K., Gibbs R., Wilson R.K.;
RL Submitted (MAR-2009) to the EMBL/GenBank/DDBJ databases.
RN [2] {ECO:0000313|Ensembl:ENSCJAP00000036867.3}
RP IDENTIFICATION.
RG Ensembl;
RL Submitted (NOV-2023) to UniProtKB.
CC -!- FUNCTION: Catalyzes the attachment of valine to tRNA(Val) in a two-step
CC reaction: valine is first activated by ATP to form Val-AMP and then
CC transferred to the acceptor end of tRNA(Val).
CC {ECO:0000256|ARBA:ARBA00043854}.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=ATP + L-valine + tRNA(Val) = AMP + diphosphate + L-valyl-
CC tRNA(Val); Xref=Rhea:RHEA:10704, Rhea:RHEA-COMP:9672, Rhea:RHEA-
CC COMP:9708, ChEBI:CHEBI:30616, ChEBI:CHEBI:33019, ChEBI:CHEBI:57762,
CC ChEBI:CHEBI:78442, ChEBI:CHEBI:78537, ChEBI:CHEBI:456215; EC=6.1.1.9;
CC Evidence={ECO:0000256|ARBA:ARBA00001624};
CC -!- SUBCELLULAR LOCATION: Mitochondrion {ECO:0000256|ARBA:ARBA00004173}.
CC -!- SIMILARITY: Belongs to the class-I aminoacyl-tRNA synthetase family.
CC {ECO:0000256|ARBA:ARBA00005594, ECO:0000256|RuleBase:RU363035}.
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DR AlphaFoldDB; F6SYV1; -.
DR STRING; 9483.ENSCJAP00000036867; -.
DR Ensembl; ENSCJAT00000038936.4; ENSCJAP00000036867.3; ENSCJAG00000019826.5.
DR GeneTree; ENSGT00940000159890; -.
DR HOGENOM; CLU_001493_0_1_1; -.
DR InParanoid; F6SYV1; -.
DR OMA; RQWYIRN; -.
DR Proteomes; UP000008225; Chromosome 4.
DR Bgee; ENSCJAG00000019826; Expressed in liver and 6 other cell types or tissues.
DR GO; GO:0005739; C:mitochondrion; IEA:UniProtKB-SubCell.
DR GO; GO:0002161; F:aminoacyl-tRNA editing activity; IEA:InterPro.
DR GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
DR GO; GO:0004832; F:valine-tRNA ligase activity; IEA:UniProtKB-EC.
DR GO; GO:0006438; P:valyl-tRNA aminoacylation; IEA:InterPro.
DR CDD; cd07962; Anticodon_Ia_Val; 1.
DR CDD; cd00817; ValRS_core; 1.
DR Gene3D; 3.40.50.620; HUPs; 2.
DR Gene3D; 3.90.740.10; Valyl/Leucyl/Isoleucyl-tRNA synthetase, editing domain; 2.
DR InterPro; IPR001412; aa-tRNA-synth_I_CS.
DR InterPro; IPR002300; aa-tRNA-synth_Ia.
DR InterPro; IPR033705; Anticodon_Ia_Val.
DR InterPro; IPR013155; M/V/L/I-tRNA-synth_anticd-bd.
DR InterPro; IPR014729; Rossmann-like_a/b/a_fold.
DR InterPro; IPR009080; tRNAsynth_Ia_anticodon-bd.
DR InterPro; IPR009008; Val/Leu/Ile-tRNA-synth_edit.
DR InterPro; IPR002303; Valyl-tRNA_ligase.
DR NCBIfam; TIGR00422; valS; 1.
DR PANTHER; PTHR11946:SF71; VALINE--TRNA LIGASE, MITOCHONDRIAL; 1.
DR PANTHER; PTHR11946; VALYL-TRNA SYNTHETASES; 1.
DR Pfam; PF08264; Anticodon_1; 1.
DR Pfam; PF00133; tRNA-synt_1; 1.
DR PRINTS; PR00986; TRNASYNTHVAL.
DR SUPFAM; SSF47323; Anticodon-binding domain of a subclass of class I aminoacyl-tRNA synthetases; 1.
DR SUPFAM; SSF52374; Nucleotidylyl transferase; 1.
DR SUPFAM; SSF50677; ValRS/IleRS/LeuRS editing domain; 1.
DR PROSITE; PS00178; AA_TRNA_LIGASE_I; 1.
PE 3: Inferred from homology;
KW Aminoacyl-tRNA synthetase {ECO:0000256|ARBA:ARBA00023146,
KW ECO:0000256|RuleBase:RU363035};
KW ATP-binding {ECO:0000256|ARBA:ARBA00022840, ECO:0000256|RuleBase:RU363035};
KW Ligase {ECO:0000256|ARBA:ARBA00022598, ECO:0000256|RuleBase:RU363035};
KW Mitochondrion {ECO:0000256|ARBA:ARBA00023128};
KW Nucleotide-binding {ECO:0000256|ARBA:ARBA00022741,
KW ECO:0000256|RuleBase:RU363035};
KW Protein biosynthesis {ECO:0000256|ARBA:ARBA00022917,
KW ECO:0000256|RuleBase:RU363035};
KW Reference proteome {ECO:0000313|Proteomes:UP000008225};
KW Transit peptide {ECO:0000256|ARBA:ARBA00022946}.
FT DOMAIN 143..764
FT /note="Aminoacyl-tRNA synthetase class Ia"
FT /evidence="ECO:0000259|Pfam:PF00133"
FT DOMAIN 809..957
FT /note="Methionyl/Valyl/Leucyl/Isoleucyl-tRNA synthetase
FT anticodon-binding"
FT /evidence="ECO:0000259|Pfam:PF08264"
FT REGION 57..101
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 68..86
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 1093 AA; 121177 MW; 14B854F45EB8BD05 CRC64;
IGGKARPRRA VGAAGGPWAE QISAPFQILL MPHLSLSSFR PPILGLRPSW GLPRFHPVST
QSEPHGSPIS RRNREAKQKR LREKQATLEA GIAGESKSPA ESIKAWSPKE VVLYEIPTKP
GEKKDVSGPL PPAYSPRYVE AAWYPWWVRE GFFKPEYQAQ LPQATGETFS MCIPPPNVTG
SLHIGHALTV AIQDALVRWH RMRGDQVLWV PGSDHAGIAT QAVVEKQLWK ERGVRRHELS
QEDFLREVWQ WKEAKGGEIY EQLQALGASL DWDRECFTMD AGSSVAVTEA FVRLHKAGLL
YRNHQLVNWS CALRSAISDI EVENRPLPGH TELRLPGCPT PVSFGLLFSV AFPVDGEPDA
EVVVGTTRPE TLPGDVAVAV HPDDSRYTHL HGRQLRHPLM GQPLPLITDC AVQPHVGTGA
VKVTPAHSPA DAEMGTRHGL SPVNVIAEDG TMTSLCGDWL QGLHRFVARE KIMSVLTERG
LFRGLQNHPM VLPICSRSGD VIEYLLKSQW FVRCQEMGAR AAQAVESGAL ELSPSFHQKS
WQHWFSHIGD WCVSRQLWWG HQIPAYLVVE DHAQGEEDCW VVGRSEAEAR EAAAELTGRP
GAELALKRDP DVLDTWFSSA LFPFSALGWP KETADLAHFY PLSLLETGSD LLLFWVGRMV
MLGTQLTGQL PFSKVLLHPM VRDRQGRKMS KSLGNVLDPR DIISGVEMQV LQEKLRSGNL
DPAELAIAAA AQKKDFPHGI PECGTDALRF TLCSHGVQGG DLRLSVSEVQ SCRHFCNKIW
NALRFILNAL GEKFVPQPAE ELSPSCPVDA WILSRLALAA RECERGFLNR ELSLVTHALH
HFWLHNLCDV YLEAVKPVLR HSPRPLGPPQ VLFSCADLGL RLLAPLMPFL AEELWQRLPP
RPGCPPAPSV SVAPYPSACS LEHWRQLELE QHFSRVQEVV QVLRALRATY QLTRARPRVL
LQSSEPGEQG LFETFLEPLA TLAHCGAVGL LPPGAAAPSG WAQAPLSDTV QVYMELQGLV
DPQIQLSLLA ARRHKLQKQL DGLIARTPSE GEAETQRQQK LSSLQLELSK LDKAVSHLRQ
LMDKPPTTGS LEL
//
